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Clinical and Developmental Immunology
Volume 2012 (2012), Article ID 820827, 9 pages
http://dx.doi.org/10.1155/2012/820827
Research Article

Fibronectin Binding Is Required for Acquisition of Mesenchymal/Endothelial Differentiation Potential in Human Circulating Monocytes

1Division of Rheumatology, Department of Internal Medicine, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-8582, Japan
2Innovative Drug Research Laboratories, Research Division, Kyowa Hakko Kirin Co., Ltd., 3 Miyahara, Takasaki, Gunma 370-1295, Japan
3Department of Biology, School of Education, Waseda University, 2-2 Wakamatsu, Shinjuku-ku, Tokyo 162-8480, Japan

Received 4 July 2012; Accepted 24 September 2012

Academic Editor: Jacek Tabarkiewicz

Copyright © 2012 Noriyuki Seta et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

We previously reported monocyte-derived multipotential cells (MOMCs), which include progenitors capable of differentiating into a variety of mesenchymal cells and endothelial cells. In vitro generation of MOMCs from circulating CD14+ monocytes requires their binding to extracellular matrix (ECM) protein and exposure to soluble factor(s) derived from circulating CD14- cells. Here, we investigated the molecular factors involved in MOMC generation by examining the binding of monocytes to ECM proteins. We found that MOMCs were obtained on the fibronectin, but not on type I collagen, laminin, or poly-L-lysine. MOMC generation was followed by changes in the expression profiles of transcription factors and was completely inhibited by either anti-α5 integrin antibody or a synthetic peptide that competed with the RGD domain for the β1-integrin binding site. These results indicate that acquisition of the multidifferentiation potential by circulating monocytes depends on their binding to the RGD domain of fibronectin via cell-surface α5β1 integrin.